J Integr Plant Biol.

• Research Article •    

Endocytosis of the damage-associated molecular pattern receptor PEPR1 is BAK1-dependent

Lucas Alves Neubus Claus1,2*, Fausto Andres Ortiz‐Morea1,2,3,4, Shao‐Li Yang1,2, Shweta Yekondi1,2, Xiangyu Xu1,2, In‐Cheol Yeo3, Isabelle Vanhoutte1,2, Nemanja Vukašinović1,2, Qian Ma1,2, Ive De Smet1,2, Ping He3, Libo Shan3 and Eugenia Russinova1,2*   

  1. 1. Department of Plant Biotechnology and Bioinformatics, Ghent University, Ghent 9052, Belgium

    2. Center for Plant Systems Biology, VIB, Ghent 9052, Belgium

    3. Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA

    4. Agricultural Engineering Program, University of the Amazon, Florencia 180002622, Colombia

    *Correspondences: Lucas Alves Neubus Claus (lucas.claus13@gmail.com); Eugenia Russinova (eurus@psb.vib-ugent.be, Dr. Russinovais fully responsible for the distribution of all materials associated with this article)

  • Received:2025-03-03 Accepted:2025-10-10 Online:2025-12-04
  • Supported by:
    This work was supported by special research funding from the Flemish Government and funding from the Student Program‐Graduate Studies Plan Program from the Coordination for the Improvement of Higher Education Personnel(Brazil) for a joint doctorate fellowship at Ghent University and University of S?o Paulo to F.A.O.‐.M., the European Union's Horizon 2020 research and innovation program under the Marie Sklodowska‐Curie grant agreement (No.101023079 ‘ENDOLOGISTIC’) to S.Y., P.E.W. Latin American Fellows Program to F.A.O.‐.M., the National Science Foundation (NSF) (MCB‐1906060) to P.H. and NSF (IOS‐2049642)to L.S., the China Scholarship Council for a predoctoral fellowship (201706350153) and a UGent BOF doctoral mandate (01CD7122) to X.X., and the Research Foundation‐Flanders (G003720N) to E.R.

Abstract: After cellular damage caused by wounding or pathogens, Arabidopsis thaliana endogenous elicitor peptides (Peps) are released into the apoplast, enhancing innate immunity by directly binding to the membrane-localized leucine-rich repeat receptor kinase PEP RECEPTOR1 (PEPR1). Ligand binding induces PEPR1 heterodimerization with the co-receptor BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1 (BAK1), followed by PEPR1 internalization, both essential for a subset of Pep1-induced responses. However, the role of BAK1 in Pep1-triggered PEPR1 endocytosis remains unclear. Here, we show that the ligand-induced PEPR1 endocytosis depends on its kinase activity and requires BAK1 C-terminal tail phosphorylation, which is equally indispensable for immune signaling and BAK1 internalization. Using a GFP insertional mutagenesis approach, we generated a partially functional GFP-tagged BAK1 to demonstrate that, following Pep1 elicitation, BAK1 and PEPR1 are endocytosed together with similar dynamics. Our findings identify the BAK1 function as a prerequisite for PEPR1 internalization.

Key words: Arabidopsis, BAK1, endocytosis, endogenous pep-tides

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